1. The Arabidopsis COBRA Protein Facilitates Cellulose Crystallization at the Plasma Membrane.

    Journal of Biological Chemistry 289(50):34911 (2014) PMID 25331944

    Mutations in the Arabidopsis COBRA gene lead to defects in cellulose synthesis but the function of COBRA is unknown. Here we present evidence that COBRA localizes to discrete particles in the plasma membrane and is sensitive to inhibitors of cellulose synthesis, suggesting that COBRA and the cel...
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  2. The Arabidopsis COBRA protein facilitates cellulose crystallization at the plasma membrane.

    Journal of Biological Chemistry 289(50):34911 (2014) PMID 25331944 PMCID PMC4263889

    Mutations in the Arabidopsis COBRA gene lead to defects in cellulose synthesis but the function of COBRA is unknown. Here we present evidence that COBRA localizes to discrete particles in the plasma membrane and is sensitive to inhibitors of cellulose synthesis, suggesting that COBRA and the cel...
  3. The Arabidopsis COBRA Protein Facilitates Cellulose Crystallization at the Plasma Membrane.

    Journal of Biological Chemistry 289(50):34911 (2014) PMID 25331944 PMCID PMC4263889

    Mutations in the Arabidopsis COBRA gene lead to defects in cellulose synthesis but the function of COBRA is unknown. Here we present evidence that COBRA localizes to discrete particles in the plasma membrane and is sensitive to inhibitors of cellulose synthesis, suggesting that COBRA and the cel...
  4. The Arabidopsis COBRA protein facilitates cellulose crystallization at the plasma membrane.

    Journal of Biological Chemistry 289(50):34911 (2014) PMID 25331944 PMCID PMC4263889

    Mutations in the Arabidopsis COBRA gene lead to defects in cellulose synthesis but the function of COBRA is unknown. Here we present evidence that COBRA localizes to discrete particles in the plasma membrane and is sensitive to inhibitors of cellulose synthesis, suggesting that COBRA and the cel...
  5. The Arabidopsis COBRA Protein Facilitates Cellulose Crystallization at the Plasma Membrane.

    Journal of Biological Chemistry 289(50):34911 (2014) PMID 25331944 PMCID PMC4263889

    Mutations in the Arabidopsis COBRA gene lead to defects in cellulose synthesis but the function of COBRA is unknown. Here we present evidence that COBRA localizes to discrete particles in the plasma membrane and is sensitive to inhibitors of cellulose synthesis, suggesting that COBRA and the cel...
  6. Analysis of protein prenylation and S-acylation using gas chromatography-coupled mass spectrometry.

    Methods in Molecular Biology 1043:121 (2013) PMID 23913042

    Lipid modifications play a key role in protein targeting and function. The two Arabidopsis Gγ subunits, AGG1 and AGG2, have been shown to undergo prenylation (AGG1) and S-acylation (AGG2). Prenylation involves covalent nonreversible attachment of either farnesyl (15 carbons) or geranylgeranyl (2...
  7. Analysis of protein prenylation and S-acylation using gas chromatography-coupled mass spectrometry.

    Methods in Molecular Biology 1043:121 (2013) PMID 23913042

    Lipid modifications play a key role in protein targeting and function. The two Arabidopsis Gγ subunits, AGG1 and AGG2, have been shown to undergo prenylation (AGG1) and S-acylation (AGG2). Prenylation involves covalent nonreversible attachment of either farnesyl (15 carbons) or geranylgeranyl (2...
  8. How prenylation and S-acylation regulate subcellular targeting and function of ROP GTPases.

    Plant Signaling & Behavior 6(7):1026 (2011) PMID 21694496 PMCID PMC3257786

    Rho of Plants (ROP) small G proteins function at discrete domains of the plasma and possibly endo membranes. ROPs are synthesized as soluble proteins and their attachment to membranes and partitioning in membrane microdomains are facilitated by the posttranslational lipid modifications prenylati...
  9. How prenylation and S-acylation regulate subcellular targeting and function of ROP GTPases.

    Plant Signaling & Behavior 6(7):1026 (2011) PMID 21694496 PMCID PMC3257786

    Rho of Plants (ROP) small G proteins function at discrete domains of the plasma and possibly endo membranes. ROPs are synthesized as soluble proteins and their attachment to membranes and partitioning in membrane microdomains are facilitated by the posttranslational lipid modifications prenylati...
  10. Differential effects of prenylation and s-acylation on type I and II ROPS membrane interaction and function.

    Plant Physiology 155(2):706 (2011) PMID 21139084 PMCID PMC3032461

    Prenylation primarily by geranylgeranylation is required for membrane attachment and function of type I Rho of Plants (ROPs) and Gγ proteins, while type II ROPs are attached to the plasma membrane by S-acylation. Yet, it is not known how prenylation affects ROP membrane interaction dynamics and ...
  11. Differential effects of prenylation and s-acylation on type I and II ROPS membrane interaction and function.

    Plant Physiology 155(2):706 (2011) PMID 21139084 PMCID PMC3032461

    Prenylation primarily by geranylgeranylation is required for membrane attachment and function of type I Rho of Plants (ROPs) and Gγ proteins, while type II ROPs are attached to the plasma membrane by S-acylation. Yet, it is not known how prenylation affects ROP membrane interaction dynamics and ...
  12. An S-acylation switch of conserved G domain cysteines is required for polarity signaling by ROP GTPases.

    Current Biology 20(10):914 (2010) PMID 20451389

    Rho GTPases are master regulators of cell polarity. For their function, Rhos must associate with discrete plasma membrane domains. Rho of Plants (ROPs) or RACs comprise a single family. Prenylation and S-acylation of hypervariable domain cysteines of Ras and Rho GTPases are required for their fu...
  13. Analysis of protein S-acylation by gas chromatography-coupled mass spectrometry using purified proteins.

    Nature Protocols 5(5):834 (2010) PMID 20379138

    S-acylation, also known as palmitoylation, involves the attachment of acyl fatty acids to thiol groups of cysteine residues through a reversible thioester bond. Owing to its reversibility, S-acylation is important in regulation of diverse signaling cascades, including Ras-associated cancers in m...
  14. Analysis of protein S-acylation by gas chromatography-coupled mass spectrometry using purified proteins.

    Nature Protocols 5(5):834 (2010) PMID 20379138

    S-acylation, also known as palmitoylation, involves the attachment of acyl fatty acids to thiol groups of cysteine residues through a reversible thioester bond. Owing to its reversibility, S-acylation is important in regulation of diverse signaling cascades, including Ras-associated cancers in m...
  15. AnS-Acylation Switch of Conserved G Domain Cysteines Is Required for Polarity Signaling by ROP GTPases

    Current Biology 20(10):914 (2010)

    Rho GTPases are master regulators of cell polarity [ 1]. For their function, Rhos must associate with discrete plasma membrane domains [ 2]. Rho of Plants (ROPs) or RACs comprise a single family [ 3–5]. Prenylation and S-acylation of hypervariable domain cysteines o...
  16. AnS-Acylation Switch of Conserved G Domain Cysteines Is Required for Polarity Signaling by ROP GTPases

    Current Biology 20(14):1326 (2010)

  17. AnS-Acylation Switch of Conserved G Domain Cysteines Is Required for Polarity Signaling by ROP GTPases

    Current Biology 20(10):914 (2010) PMID 20451389

    Rho GTPases are master regulators of cell polarity [ 1]. For their function, Rhos must associate with discrete plasma membrane domains [ 2]. Rho of Plants (ROPs) or RACs comprise a single family [ 3–5]. Prenylation and S-acylation of hypervariable domain cysteines o...
  18. AnS-Acylation Switch of Conserved G Domain Cysteines Is Required for Polarity Signaling by ROP GTPases

    Current Biology 20(10):914 (2010) PMID 20451389

    Rho GTPases are master regulators of cell polarity [ 1]. For their function, Rhos must associate with discrete plasma membrane domains [ 2]. Rho of Plants (ROPs) or RACs comprise a single family [ 3–5]. Prenylation and S-acylation of hypervariable domain cysteines o...
  19. Protein lipid modifications in signaling and subcellular targeting.

    Current Opinion in Plant Biology 12(6):714 (2009) PMID 19796984

    Classically perceived as means for recruiting proteins to the membranes, protein lipid modifications are known today to play diverse roles in subcellular targeting, protein-protein interactions and signaling. This review focuses on three protein lipid modifications: prenylation, S-acylation and ...
  20. Protein lipid modifications in signaling and subcellular targeting.

    Current Opinion in Plant Biology 12(6):714 (2009) PMID 19796984

    Classically perceived as means for recruiting proteins to the membranes, protein lipid modifications are known today to play diverse roles in subcellular targeting, protein-protein interactions and signaling. This review focuses on three protein lipid modifications: prenylation, S-acylation and ...